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Record Information
Version2.0
Creation Date2009-07-30 17:55:46 UTC
Update Date2014-12-24 20:26:00 UTC
Accession NumberT3D3125
Identification
Common NameBotulinum neurotoxin type B
ClassProtein
DescriptionBotulinum toxin is a neurotoxic protein produced by the bacterium Clostridium botulinum. Though it is the most toxic protein known, it may be used in minute doses to treat muscle spasms and in cosmetic treatment, under the brand name Botox. (2)
Compound Type
  • Amide
  • Amine
  • Bacterial Toxin
  • Botulinal Neurotoxin
  • Natural Compound
  • Organic Compound
  • Protein
Protein StructureT3d3125
Synonyms
Synonym
BoNT/B
Bontoxilysin-B
Chemical FormulaNot Available
Average Molecular Mass150801.160 g/mol
CAS Registry NumberNot Available
SequenceNot Available
Chemical Taxonomy
DescriptionNot Available
KingdomOrganic Compounds
Super ClassOrganic Acids
ClassCarboxylic Acids and Derivatives
Sub ClassAmino Acids, Peptides, and Analogues
Direct ParentPeptides
Alternative ParentsNot Available
SubstituentsNot Available
Molecular FrameworkNot Available
External DescriptorsNot Available
Biological Properties
StatusDetected and Not Quantified
OriginExogenous
Cellular LocationsNot Available
Biofluid LocationsNot Available
Tissue LocationsNot Available
PathwaysNot Available
ApplicationsNot Available
Biological RolesNot Available
Chemical RolesNot Available
Physical Properties
StateLiquid
AppearanceClear solution.
Experimental Properties
PropertyValue
Melting PointNot Available
Boiling PointNot Available
Solubility>10 mg/mL
LogPNot Available
Predicted PropertiesNot Available
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyDeposition DateView
Toxicity Profile
Route of ExposureOral (4) ; inhalation (4) ; dermal (4)
Mechanism of ToxicityBotulinum toxin is a two-chain polypeptide with a 100-kDa heavy chain joined by a disulfide bond to a 50-kDa light chain. Following the attachment of the toxin heavy chain to proteins on the surface of axon terminals, the toxin can be taken into neurons by endocytosis. The light chain is able to cleave endocytotic vesicles and reach the cytoplasm. The light chain has protease activity and proteolytically degrades the SNAP-25 protein at neuromuscular junctions, preventing vesicles from anchoring to the membrane to release acetylcholine. By inhibiting acetylcholine release, the toxin interferes with nerve impulses and causes flaccid (sagging) paralysis of muscles. (2)
MetabolismFree toxin may be removed by opsonization via the reticuloendothelial system (primarily the liver and kidneys) or it may be degraded through cellular internalization via the lysosomes. Lysosomes are membrane-enclosed organelles that contain an array of digestive enzymes, including several proteases.
Toxicity ValuesLD50: 1.2 ng/mg (Intraperitoneal, Mouse) (1)
Lethal Dose1 nanogram/kg for an adult human. (2)
Carcinogenicity (IARC Classification)No indication of carcinogenicity to humans (not listed by IARC).
Uses/SourcesBotulinum toxin is a neurotoxic protein produced by the bacterium Clostridium botulinum. Though it is the most toxic protein known, it may be used in minute doses to treat muscle spasms and in cosmetic treatment, under the brand name Botox. (2)
Minimum Risk LevelNot Available
Health EffectsBotulinum toxin is an extremely potent neurotoxin that causes paralysis. Death may result from respiratory failure following paralysis of the respiratory muscles. (2)
SymptomsAdverse effects from the cosmetic use of botulinum toxin include headaches, focal facial paralysis, muscle weakness, dysphagia, flu-like syndromes, and allergic reactions. (2)
TreatmentTreatment consists of antitoxin administration and artificial ventilation until the neurotoxins are excreted or metabolised. The two primary botulinum antitoxins are Trivalent (A,B,E) Botulinum Antitoxin and Heptavalent (A,B,C,D,E,F,G) Botulinum Antitoxin. (2)
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDNot Available
HMDB IDNot Available
PubChem Compound IDNot Available
ChEMBL IDNot Available
ChemSpider IDNot Available
KEGG IDNot Available
UniProt IDP10844
OMIM ID
ChEBI IDNot Available
BioCyc IDNot Available
CTD IDNot Available
Stitch IDBotulinum neurotoxin type B
PDB ID1EPW
ACToR IDNot Available
Wikipedia LinkNot Available
References
Synthesis ReferenceNot Available
MSDST3D3125.pdf
General References
  1. Gill DM: Bacterial toxins: a table of lethal amounts. Microbiol Rev. 1982 Mar;46(1):86-94. [6806598 ]
  2. Wikipedia. Botulinum toxin. Last Updated 12 August 2009. [Link]
  3. Wikipedia. Bacterial toxin. Last Updated 27 February 2009. [Link]
  4. ATSDR - Agency for Toxic Substances and Disease Registry (1999). Toxicological profile for uranium. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
Gene Regulation
Up-Regulated GenesNot Available
Down-Regulated GenesNot Available